Physicochemical characterisation of dihydro-alpha-lipoic acid interaction with human serum albumin by multi-spectroscopic and molecular modelling approaches
Authors
Gligorijević, Nikola![](/themes/MirageCherry/images/orcid.png)
Šukalović, Vladimir
![](/themes/MirageCherry/images/orcid.png)
Minić, Simeon L.
![](/themes/MirageCherry/images/orcid.png)
Miljuš, Goran
Nedić, Olgica
![](/themes/MirageCherry/images/orcid.png)
Penezić, Ana Z.
![](/themes/MirageCherry/images/orcid.png)
Article (Published version)
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The binding of a popular food supplement and well-known antioxidant, dihydro-alpha-lipoic acid (DHLA) to human serum albumin (HSA) was characterised. The binding was monitored by several spectroscopic methods together with the molecular docking approach. HSA was able to bind DHLA with moderate affinity, 1.00±0.05×104 M-1. Spectroscopic data demonstrated that the preferential binding site for DHLA on HSA is IIA (Sudlow I). Both experimental and molecular docking analysis identified electrostatic (salt bridges) and hydrogen bonds as the key interactions involved in DHLA binding to HSA. Molecular docking confirmed that the Sudlow I site could accommodate DHLA and that the ligand is bound to the protein in a specific conformation. The molecular dynamic simulation showed that the formed complex is stable. Binding of DHLA does not affect the structure of the protein, but it thermally stabilises HSA. Bound DHLA had no effect on the susceptibility of HSA to trypsin digestion. Since DHLA is a c...ommonly used food supplement, knowledge of its pharmacokinetics and pharmacodynamic properties in an organism is very important. This study further expands it by providing a detailed analysis of its interaction with HSA, the primary drug transporter in the circulation.
Keywords:
spectral analysis / molecular docking / protein-ligand interaction / protein stability / protein structureSource:
Journal of the Serbian Chemical Society, 2021, 86, 9, 795-807Publisher:
- Belgrade : Serbian Chemical Society
Funding / projects:
- Ministry of Science, Technological Development and Innovation of the Republic of Serbia, institutional funding - 200019 (University of Belgrade, Institute for the Application of Nuclear Energy - INEP) (RS-MESTD-inst-2020-200019)
- Ministry of Science, Technological Development and Innovation of the Republic of Serbia, institutional funding - 200026 (University of Belgrade, Institute of Chemistry, Technology and Metallurgy - IChTM) (RS-MESTD-inst-2020-200026)
- Ministry of Science, Technological Development and Innovation of the Republic of Serbia, institutional funding - 200168 (University of Belgrade, Faculty of Chemistry) (RS-MESTD-inst-2020-200168)
DOI: 10.2298/JSC210420041G
ISSN: 0352-5139
WoS: 000692558700002
Scopus: 2-s2.0-85114223943
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Hemijski fakultet / Faculty of ChemistryTY - JOUR AU - Gligorijević, Nikola AU - Šukalović, Vladimir AU - Minić, Simeon L. AU - Miljuš, Goran AU - Nedić, Olgica AU - Penezić, Ana Z. PY - 2021 UR - https://cherry.chem.bg.ac.rs/handle/123456789/4667 AB - The binding of a popular food supplement and well-known antioxidant, dihydro-alpha-lipoic acid (DHLA) to human serum albumin (HSA) was characterised. The binding was monitored by several spectroscopic methods together with the molecular docking approach. HSA was able to bind DHLA with moderate affinity, 1.00±0.05×104 M-1. Spectroscopic data demonstrated that the preferential binding site for DHLA on HSA is IIA (Sudlow I). Both experimental and molecular docking analysis identified electrostatic (salt bridges) and hydrogen bonds as the key interactions involved in DHLA binding to HSA. Molecular docking confirmed that the Sudlow I site could accommodate DHLA and that the ligand is bound to the protein in a specific conformation. The molecular dynamic simulation showed that the formed complex is stable. Binding of DHLA does not affect the structure of the protein, but it thermally stabilises HSA. Bound DHLA had no effect on the susceptibility of HSA to trypsin digestion. Since DHLA is a commonly used food supplement, knowledge of its pharmacokinetics and pharmacodynamic properties in an organism is very important. This study further expands it by providing a detailed analysis of its interaction with HSA, the primary drug transporter in the circulation. PB - Belgrade : Serbian Chemical Society T2 - Journal of the Serbian Chemical Society T1 - Physicochemical characterisation of dihydro-alpha-lipoic acid interaction with human serum albumin by multi-spectroscopic and molecular modelling approaches VL - 86 IS - 9 SP - 795 EP - 807 DO - 10.2298/JSC210420041G ER -
@article{ author = "Gligorijević, Nikola and Šukalović, Vladimir and Minić, Simeon L. and Miljuš, Goran and Nedić, Olgica and Penezić, Ana Z.", year = "2021", abstract = "The binding of a popular food supplement and well-known antioxidant, dihydro-alpha-lipoic acid (DHLA) to human serum albumin (HSA) was characterised. The binding was monitored by several spectroscopic methods together with the molecular docking approach. HSA was able to bind DHLA with moderate affinity, 1.00±0.05×104 M-1. Spectroscopic data demonstrated that the preferential binding site for DHLA on HSA is IIA (Sudlow I). Both experimental and molecular docking analysis identified electrostatic (salt bridges) and hydrogen bonds as the key interactions involved in DHLA binding to HSA. Molecular docking confirmed that the Sudlow I site could accommodate DHLA and that the ligand is bound to the protein in a specific conformation. The molecular dynamic simulation showed that the formed complex is stable. Binding of DHLA does not affect the structure of the protein, but it thermally stabilises HSA. Bound DHLA had no effect on the susceptibility of HSA to trypsin digestion. Since DHLA is a commonly used food supplement, knowledge of its pharmacokinetics and pharmacodynamic properties in an organism is very important. This study further expands it by providing a detailed analysis of its interaction with HSA, the primary drug transporter in the circulation.", publisher = "Belgrade : Serbian Chemical Society", journal = "Journal of the Serbian Chemical Society", title = "Physicochemical characterisation of dihydro-alpha-lipoic acid interaction with human serum albumin by multi-spectroscopic and molecular modelling approaches", volume = "86", number = "9", pages = "795-807", doi = "10.2298/JSC210420041G" }
Gligorijević, N., Šukalović, V., Minić, S. L., Miljuš, G., Nedić, O.,& Penezić, A. Z.. (2021). Physicochemical characterisation of dihydro-alpha-lipoic acid interaction with human serum albumin by multi-spectroscopic and molecular modelling approaches. in Journal of the Serbian Chemical Society Belgrade : Serbian Chemical Society., 86(9), 795-807. https://doi.org/10.2298/JSC210420041G
Gligorijević N, Šukalović V, Minić SL, Miljuš G, Nedić O, Penezić AZ. Physicochemical characterisation of dihydro-alpha-lipoic acid interaction with human serum albumin by multi-spectroscopic and molecular modelling approaches. in Journal of the Serbian Chemical Society. 2021;86(9):795-807. doi:10.2298/JSC210420041G .
Gligorijević, Nikola, Šukalović, Vladimir, Minić, Simeon L., Miljuš, Goran, Nedić, Olgica, Penezić, Ana Z., "Physicochemical characterisation of dihydro-alpha-lipoic acid interaction with human serum albumin by multi-spectroscopic and molecular modelling approaches" in Journal of the Serbian Chemical Society, 86, no. 9 (2021):795-807, https://doi.org/10.2298/JSC210420041G . .